dbPTM

MK08_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MK08_HUMAN
UniProt AC	P45983
Protein Name	Mitogen-activated protein kinase 8
Gene Name	MAPK8
Organism	Homo sapiens (Human).
Sequence Length	427
Subcellular Localization	Cytoplasm . Nucleus . Colocalizes with POU5F1 in the nucleus.
Protein Description	Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. [PubMed: 22441692 Phosphorylates the heat shock transcription factor HSF1, suppressing HSF1-induced transcriptional activity]
Protein Sequence	MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEERTKNGVIRGQPSPLGAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	YSVEIGDSTFTVLKR EEEEECCCHHHHHHH	21.87	29759185
19	Phosphorylation	SVEIGDSTFTVLKRY EEEECCCHHHHHHHH	28.23	29759185
21	Phosphorylation	EIGDSTFTVLKRYQN EECCCHHHHHHHHCC	25.64	29759185
30	Ubiquitination	LKRYQNLKPIGSGAQ HHHHCCCCCCCCCCC	41.98	-
56	Ubiquitination	ERNVAIKKLSRPFQN HHCHHHHHHCCCCCC	45.65	-
68	Ubiquitination	FQNQTHAKRAYRELV CCCHHHHHHHHHHHH	29.92	-
116	S-nitrosocysteine	ELMDANLCQVIQMEL HHCCCCHHHHHHCCC	2.81	-
116	S-nitrosylation	ELMDANLCQVIQMEL HHCCCCHHHHHHCCC	2.81	22178444
129	Phosphorylation	ELDHERMSYLLYQML CCCHHHHHHHHHHHH	20.89	24043423
130	Phosphorylation	LDHERMSYLLYQMLC CCHHHHHHHHHHHHH	7.44	24043423
133	Phosphorylation	ERMSYLLYQMLCGIK HHHHHHHHHHHHCHH	6.84	24043423
144	Phosphorylation	CGIKHLHSAGIIHRD HCHHHHHHCCEECCC	34.25	-
153	Ubiquitination	GIIHRDLKPSNIVVK CEECCCCCHHHEEEE	51.17	-
155	Phosphorylation	IHRDLKPSNIVVKSD ECCCCCHHHEEEECC	37.29	22817900
160	Ubiquitination	KPSNIVVKSDCTLKI CHHHEEEECCCEEEE	29.68	-
166	Ubiquitination	VKSDCTLKILDFGLA EECCCEEEECCHHCC	24.06	-
175	Phosphorylation	LDFGLARTAGTSFMM CCHHCCCCCCCCCCC	24.67	21945579
178	Phosphorylation	GLARTAGTSFMMTPY HCCCCCCCCCCCCCH	19.14	21945579
179	Phosphorylation	LARTAGTSFMMTPYV CCCCCCCCCCCCCHH	15.38	21945579
183 (in isoform 2)	Phosphorylation	-	10.32	18669648
183	Phosphorylation	AGTSFMMTPYVVTRY CCCCCCCCCHHEEEH	10.32	22322096
185 (in isoform 2)	Phosphorylation	-	9.82	18669648
185	Phosphorylation	TSFMMTPYVVTRYYR CCCCCCCHHEEEHHC	9.82	22322096
188	Phosphorylation	MMTPYVVTRYYRAPE CCCCHHEEEHHCCCH	11.69	21945579
224	Ubiquitination	EMVCHKILFPGRDYI HHHHHHHHCCCHHHH	5.16	21906983
228 (in isoform 4)	Phosphorylation	-	33.52	-
228 (in isoform 3)	Phosphorylation	-	33.52	-
243	Phosphorylation	KVIEQLGTPCPEFMK HHHHHHCCCCHHHHH	30.25	-
250	Ubiquitination	TPCPEFMKKLQPTVR CCCHHHHHHHCCCHH	56.50	-
251	Ubiquitination	PCPEFMKKLQPTVRT CCHHHHHHHCCCHHH	40.33	-
255	Phosphorylation	FMKKLQPTVRTYVEN HHHHHCCCHHHHHHC	15.06	17924679
258	Phosphorylation	KLQPTVRTYVENRPK HHCCCHHHHHHCCCC	27.81	17924679
259	Phosphorylation	LQPTVRTYVENRPKY HCCCHHHHHHCCCCC	8.66	17924679
265	Ubiquitination	TYVENRPKYAGYSFE HHHHCCCCCCCCCHH	44.49	-
273	Ubiquitination	YAGYSFEKLFPDVLF CCCCCHHHHCCCCCC	54.11	-
284	Phosphorylation	DVLFPADSEHNKLKA CCCCCCCCHHCCCCH	42.75	-
288	Ubiquitination	PADSEHNKLKASQAR CCCCHHCCCCHHHHH	53.96	-
290	Ubiquitination	DSEHNKLKASQARDL CCHHCCCCHHHHHHH	47.83	-
292	Phosphorylation	EHNKLKASQARDLLS HHCCCCHHHHHHHHH	23.84	-
300	Ubiquitination	QARDLLSKMLVIDAS HHHHHHHHHHHHCHH	35.90	2190698
300 (in isoform 1)	Ubiquitination	-	35.90	21906983
300 (in isoform 2)	Ubiquitination	-	35.90	21906983
300 (in isoform 3)	Ubiquitination	-	35.90	21906983
300 (in isoform 4)	Ubiquitination	-	35.90	21906983
301 (in isoform 5)	Phosphorylation	-	3.04	30266825
308	Ubiquitination	MLVIDASKRISVDEA HHHHCHHHCCCHHHH	56.31	19608861
308	Acetylation	MLVIDASKRISVDEA HHHHCHHHCCCHHHH	56.31	23236377
336	Ubiquitination	EAEAPPPKIPDKQLD HCCCCCCCCCHHHCC	73.05	-
353	Ubiquitination	EHTIEEWKELIYKEV CHHHHHHHHHHHHHH	46.02	-
357	Phosphorylation	EEWKELIYKEVMDLE HHHHHHHHHHHCCHH	17.45	17924679
367	Phosphorylation	VMDLEERTKNGVIRG HCCHHHHHHCCCCCC	31.94	17924679
377 (in isoform 2)	Phosphorylation	-	25.52	30266825
377 (in isoform 3)	Phosphorylation	-	25.52	30266825
377	Phosphorylation	GVIRGQPSPLGAAVI CCCCCCCCCCCEEEE	25.52	15345747

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
183	T	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
183	T	Phosphorylation	Kinase	MAP3K6	O95382	GPS
183	T	Phosphorylation	Kinase	MAP2K4	P45985	GPS
183	T	Phosphorylation	Kinase	MAP2K4	P45985	GPS
183	T	Phosphorylation	Kinase	MP2K7	O14733	PhosphoELM
183	T	Phosphorylation	Kinase	MAP2K7	O14733	GPS
185	Y	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
185	Y	Phosphorylation	Kinase	MAP3K6	O95382	GPS
185	Y	Phosphorylation	Kinase	MP2K4	P45985	PhosphoELM
185	Y	Phosphorylation	Kinase	MAP2K4	P45985	GPS
185	Y	Phosphorylation	Kinase	MAP2K4	P45985	GPS
185	Y	Phosphorylation	Kinase	MAP2K7	O14733	GPS
185	Y	Phosphorylation	Kinase	RET	P07949	PSP
228	T	Phosphorylation	Kinase	MAP2K4	P45985	GPS
284	S	Phosphorylation	Kinase	MAP2K4	P45985	GPS
377	S	Phosphorylation	Kinase	MAP2K4	P45985	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:20581839

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
183	T	Phosphorylation	7839144
Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme.
183	T	Phosphorylation	7839144
May be phosphorylated at Thr-183 and Tyr-185 by MAP3K1/MEKK1.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of MK08_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IRS1_HUMAN	IRS1	physical	11606564
TR10B_HUMAN	TNFRSF10B	physical	15659383
FADD_HUMAN	FADD	physical	15659383
TNFL6_HUMAN	FASLG	physical	15659383
CASPA_HUMAN	CASP10	physical	15659383
CASP8_HUMAN	CASP8	physical	15659383
TNR1A_HUMAN	TNFRSF1A	physical	15659383
JUN_HUMAN	JUN	physical	14633987
SPIB_HUMAN	SPIB	physical	8632909
SPI1_HUMAN	SPI1	physical	8632909
3BP5_HUMAN	SH3BP5	physical	12167088
JUN_HUMAN	JUN	physical	9774977
M3K1_HUMAN	MAP3K1	physical	9405400
ELP1_HUMAN	IKBKAP	physical	12058026
KPCD1_HUMAN	PRKD1	physical	11948398
CRK_HUMAN	CRK	physical	11432831
BCAR1_HUMAN	BCAR1	physical	11432831
JUN_HUMAN	JUN	physical	8137421
KS6B1_MOUSE	Rps6kb1	physical	11279232
IRS1_HUMAN	IRS1	physical	10722755
SH23A_HUMAN	SH2D3A	genetic	10187783
JUN_HUMAN	JUN	physical	11479302
PAX2_HUMAN	PAX2	physical	11700324
P53_MOUSE	Trp53	physical	9393873
P53_HUMAN	TP53	physical	9393873
JIP3_HUMAN	MAPK8IP3	physical	10629060
JUN_HUMAN	JUN	physical	8621542
REL_HUMAN	REL	physical	8621542
JUNB_HUMAN	JUNB	physical	9405416
ATF2_HUMAN	ATF2	physical	9405416
ETV1_HUMAN	ETV1	physical	11551945
ELK1_HUMAN	ELK1	physical	8586671
JUN_HUMAN	JUN	physical	8586671
DUS1_HUMAN	DUSP1	physical	11278799
ATF2_HUMAN	ATF2	physical	11279118
MP2K7_HUMAN	MAP2K7	physical	9207092
ATF2_HUMAN	ATF2	physical	9207092
MP2K4_HUMAN	MAP2K4	genetic	9207092
MP2K7_HUMAN	MAP2K7	genetic	9207092
GSTP1_HUMAN	GSTP1	physical	11279197
MYC_HUMAN	MYC	physical	10551811
NR4A1_HUMAN	NR4A1	physical	17023523
CEBPA_HUMAN	CEBPA	physical	16983342
CDN1A_HUMAN	CDKN1A	physical	20102411
SIR1_HUMAN	SIRT1	physical	20027304
JUN_HUMAN	JUN	physical	16740711
H2AX_HUMAN	H2AFX	physical	17145805
P53_HUMAN	TP53	physical	15538975
HDAC9_HUMAN	HDAC9	physical	16611996
JUND_HUMAN	JUND	physical	16264271
TFCP2_HUMAN	TFCP2	physical	15857981
NFAC2_HUMAN	NFATC2	physical	15184502
NFE2_HUMAN	NFE2	physical	19966288
P53_HUMAN	TP53	physical	9724739
H2AX_HUMAN	H2AFX	physical	20512932
ATF2_HUMAN	ATF2	physical	12958075
P53_HUMAN	TP53	physical	19651615
PIAS2_HUMAN	PIAS2	physical	19815509
ZN605_HUMAN	ZNF605	physical	21900206
DUS8_HUMAN	DUSP8	physical	21900206
F193B_HUMAN	FAM193B	physical	21900206
BMPR2_HUMAN	BMPR2	physical	21900206
PNRC1_HUMAN	PNRC1	physical	21900206
HSP7C_HUMAN	HSPA8	physical	21900206
DAPLE_HUMAN	CCDC88C	physical	21900206
ZN219_HUMAN	ZNF219	physical	21900206
RBM15_HUMAN	RBM15	physical	21900206
SCND1_HUMAN	SCAND1	physical	21900206
JUN_HUMAN	JUN	physical	10419510
STAT3_HUMAN	STAT3	physical	10521505
K2C8_HUMAN	KRT8	physical	11781324
NCOA3_HUMAN	NCOA3	physical	15383283
ATF2_HUMAN	ATF2	physical	21444723
CBL_HUMAN	CBL	physical	11944898
JUN_HUMAN	JUN	physical	18957422
JUN_HUMAN	JUN	physical	10962563
JUN_HUMAN	JUN	physical	15590691
FZR1_HUMAN	FZR1	physical	20581839
JUN_HUMAN	JUN	physical	15958389
ITCH_HUMAN	ITCH	physical	16446428
RAD18_HUMAN	RAD18	physical	22456510
FLNB_HUMAN	FLNB	physical	19270716
JUN_HUMAN	JUN	physical	19270716
P53_HUMAN	TP53	physical	18813780
JUN_HUMAN	JUN	physical	18922473
JUN_HUMAN	JUN	physical	15299005
M3K1_HUMAN	MAP3K1	physical	15299005
JUN_HUMAN	JUN	physical	16157600
RPTOR_HUMAN	RPTOR	physical	22493283
MTOR_HUMAN	MTOR	physical	22493283
M3K7_HUMAN	MAP3K7	physical	11865055
JUN_HUMAN	JUN	physical	9575168
JUN_HUMAN	JUN	physical	12185592
JUN_HUMAN	JUN	physical	9692890
TRAF2_HUMAN	TRAF2	physical	9692890
JUN_HUMAN	JUN	physical	14572659
ATF2_HUMAN	ATF2	physical	12874243
JUN_HUMAN	JUN	physical	16434970
NR4A1_HUMAN	NR4A1	physical	14612408
JUN_HUMAN	JUN	physical	14612408
JUN_HUMAN	JUN	physical	14517282
GSTP1_HUMAN	GSTP1	physical	16636664
JUN_HUMAN	JUN	physical	20133937
JUN_HUMAN	JUN	physical	12228228
ATF2_HUMAN	ATF2	physical	12804775
ATF2_HUMAN	ATF2	physical	9162092
JUN_HUMAN	JUN	physical	20732415
MK08_HUMAN	MAPK8	physical	20194509
BCL2_HUMAN	BCL2	physical	15733859
JUN_HUMAN	JUN	physical	9808624
JUN_HUMAN	JUN	physical	15749833
ATF2_HUMAN	ATF2	physical	9399639
JUN_HUMAN	JUN	physical	16533805
MP2K4_HUMAN	MAP2K4	physical	16533805
JIP1_HUMAN	MAPK8IP1	physical	16533805
MP2K7_HUMAN	MAP2K7	physical	16533805
MP2K1_HUMAN	MAP2K1	physical	16533805
MP2K2_HUMAN	MAP2K2	physical	16533805
JUN_HUMAN	JUN	physical	11108663
P53_HUMAN	TP53	physical	11108663
JIP1_HUMAN	MAPK8IP1	physical	15998799
CTNB1_HUMAN	CTNNB1	physical	19667122
STAB2_HUMAN	STAB2	physical	18387958
JUN_HUMAN	JUN	physical	22110360
CDN1B_HUMAN	CDKN1B	physical	12963725
JUN_HUMAN	JUN	physical	12963725
JUN_HUMAN	JUN	physical	19527717
A4_HUMAN	APP	physical	21832049
JUN_HUMAN	JUN	physical	10747973
HSF1_HUMAN	HSF1	physical	10747973
JUN_HUMAN	JUN	physical	8654373
ATF2_HUMAN	ATF2	physical	8654373
ELK1_HUMAN	ELK1	physical	8654373
GORS2_HUMAN	GORASP2	physical	11408587
JUN_HUMAN	JUN	physical	13130464
JUN_HUMAN	JUN	physical	8001819
WDR62_HUMAN	WDR62	physical	19910486
JUN_HUMAN	JUN	physical	19910486
DCP1A_HUMAN	DCP1A	physical	19910486
JUN_HUMAN	JUN	physical	17189706
RARA_MOUSE	Rara	physical	10383391
IRF3_HUMAN	IRF3	physical	19153595
AIMP1_HUMAN	AIMP1	physical	20510162
ELK4_HUMAN	ELK4	physical	9020136
B2L11_HUMAN	BCL2L11	physical	12591950
BMF_HUMAN	BMF	physical	12591950
JUN_HUMAN	JUN	physical	15677475
JKAMP_HUMAN	JKAMP	physical	16166642
JUN_HUMAN	JUN	physical	16166642
DUS10_HUMAN	DUSP10	physical	16166642
SIN1_HUMAN	MAPKAP1	physical	15722200
JUN_HUMAN	JUN	physical	16824735
NFAC4_HUMAN	NFATC4	physical	17875713
NFAC3_HUMAN	NFATC3	physical	17875713
ELK1_HUMAN	ELK1	physical	17875713
JUN_HUMAN	JUN	physical	17875713
ATF2_HUMAN	ATF2	physical	17875713
PMYT1_HUMAN	PKMYT1	physical	19204086
JUN_HUMAN	JUN	physical	17363973
JUN_HUMAN	JUN	physical	18429822
JUN_HUMAN	JUN	physical	8846788
ELK1_HUMAN	ELK1	physical	8846788
SPB3_HUMAN	SERPINB3	physical	16549498
JUN_HUMAN	JUN	physical	16549498
CDN2A_HUMAN	CDKN2A	physical	16007099
ARF_HUMAN	CDKN2A	physical	16007099
CDN2C_HUMAN	CDKN2C	physical	16007099
JUN_HUMAN	JUN	physical	16007099
JUN_HUMAN	JUN	physical	12697749
JUN_HUMAN	JUN	physical	11278395
JUN_HUMAN	JUN	physical	16291755
WWOX_MOUSE	Wwox	physical	12514174
P53_HUMAN	TP53	physical	12514174
WWOX_HUMAN	WWOX	physical	12514174
JUN_HUMAN	JUN	physical	18003900
TAU_HUMAN	MAPT	physical	9199504
A4_HUMAN	APP	physical	12917434
APLP2_HUMAN	APLP2	physical	12917434
GEMI5_HUMAN	GEMIN5	physical	17541429
SSU72_HUMAN	SSU72	physical	21988832
SCOC_HUMAN	SCOC	physical	21988832
MKNK2_HUMAN	MKNK2	physical	21988832
RAF1_HUMAN	RAF1	physical	21988832
RLA2_HUMAN	RPLP2	physical	21988832
KS6B1_HUMAN	RPS6KB1	physical	21988832
MK08_HUMAN	MAPK8	physical	23602568
KS6B1_HUMAN	RPS6KB1	physical	23816567
JUN_HUMAN	JUN	physical	23816567
JUN_HUMAN	JUN	physical	11907583
1433Z_HUMAN	YWHAZ	physical	15696159
ATF2_HUMAN	ATF2	physical	11865055
SP1_HUMAN	SP1	physical	25398907
EP300_HUMAN	EP300	physical	11278389
JIP1_HUMAN	MAPK8IP1	physical	16343492
AKT1_HUMAN	AKT1	physical	20186153
TCPB_HUMAN	CCT2	physical	25852190
TCPG_HUMAN	CCT3	physical	25852190
TCPD_HUMAN	CCT4	physical	25852190
TCPZ_HUMAN	CCT6A	physical	25852190
TCPQ_HUMAN	CCT8	physical	25852190
NUP98_HUMAN	NUP98	physical	25852190
TCPA_HUMAN	TCP1	physical	25852190
TKT_HUMAN	TKT	physical	25852190
SUN2_HUMAN	SUN2	physical	25852190
P53_HUMAN	TP53	physical	9732264
MK09_HUMAN	MAPK9	physical	26186194
WDR62_HUMAN	WDR62	physical	26186194
ATE1_HUMAN	ATE1	physical	26186194
KCAB3_HUMAN	KCNAB3	physical	26186194
DUS8_HUMAN	DUSP8	physical	26186194
PPM1B_HUMAN	PPM1B	physical	26344197
ANXA7_HUMAN	ANXA7	physical	26496610
BCL7A_HUMAN	BCL7A	physical	26496610
BLMH_HUMAN	BLMH	physical	26496610
CATC_HUMAN	CTSC	physical	26496610
CSK22_HUMAN	CSNK2A2	physical	26496610
M3K4_HUMAN	MAP3K4	physical	26496610
PSMD2_HUMAN	PSMD2	physical	26496610
SF01_HUMAN	SF1	physical	26496610
H2A2A_HUMAN	HIST2H2AA3	physical	26496610
ZO2_HUMAN	TJP2	physical	26496610
COG2_HUMAN	COG2	physical	26496610
PHLP1_HUMAN	PHLPP1	physical	26496610
CRTC3_HUMAN	CRTC3	physical	26496610
TAF1D_HUMAN	TAF1D	physical	26496610
WDCP_HUMAN	C2orf44	physical	26496610
PRR3_HUMAN	PRR3	physical	26496610
S11IP_HUMAN	STK11IP	physical	26496610
RABL3_HUMAN	RABL3	physical	26496610
MP2K7_HUMAN	MAP2K7	physical	25241761
TNFL6_HUMAN	FASLG	physical	25241761
RHOA_HUMAN	RHOA	physical	25241761
M3K1_HUMAN	MAP3K1	physical	25241761
B2CL1_HUMAN	BCL2L1	physical	25241761
SMAD3_HUMAN	SMAD3	physical	25241761
JUN_HUMAN	JUN	physical	14557262
JUN_HUMAN	JUN	physical	12832416
MBP_HUMAN	MBP	physical	10978313
JUN_HUMAN	JUN	physical	15289320
JUN_HUMAN	JUN	physical	10987838
GSTP1_HUMAN	GSTP1	physical	26429914
JUN_HUMAN	JUN	physical	25098452
MK09_HUMAN	MAPK9	physical	28514442
DUS8_HUMAN	DUSP8	physical	28514442
KCAB3_HUMAN	KCNAB3	physical	28514442
WDR62_HUMAN	WDR62	physical	28514442
ATE1_HUMAN	ATE1	physical	28514442
B2CL1_HUMAN	BCL2L1	physical	22617334
JUN_HUMAN	JUN	physical	10464310
JUN_HUMAN	JUN	physical	10908726
JUN_HUMAN	JUN	physical	12149229
JUN_HUMAN	JUN	physical	22904686
CDN1A_HUMAN	CDKN1A	physical	12058028
JUN_HUMAN	JUN	physical	15143066

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MK08_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-308, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; THR-183; TYR-185AND SER-377, AND MASS SPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183; TYR-185 ANDSER-377, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, ANDMASS SPECTROMETRY.	17192257 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255; THR-258; TYR-259;TYR-357 AND THR-367, AND MASS SPECTROMETRY.	17924679 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, AND MASSSPECTROMETRY.	18083107 [Abstract]

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